Anti-HSP-70 (11108-100ul)

Hsp70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides. Hsp70 recognizes and binds to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound protein. The ability of Hsp70 to undergo cycles of binding and release from hydrophobic stretches of partially unfolded proteins is the basis for their role in a variety of intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport.